4H2L

Deer mouse hemoglobin in hydrated format

4H2L の概要

• エントリーDOI: 10.2210/pdb4h2l/pdb
• 分子名称: Alpha-globin, Beta globin, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: hemoglobin, oxygen transport
• 由来する生物種: Peromyscus maniculatus (North American deer mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32035.24

構造登録者

Inoguchi, N.,Oshlo, J.R.,Natarajan, C.,Weber, R.E.,Fago, A.,Storz, J.F.,Moriyama, H. (登録日: 2012-09-12, 公開日: 2013-04-10, 最終更新日: 2024-02-28)

主引用文献

Inoguchi, N.,Oshlo, J.R.,Natarajan, C.,Weber, R.E.,Fago, A.,Storz, J.F.,Moriyama, H.
Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix.
Acta Crystallogr.,Sect.F, 69:393-398, 2013

PubMed Abstract: The deer mouse, Peromyscus maniculatus, exhibits altitude-associated variation in hemoglobin oxygen affinity. To examine the structural basis of this functional variation, the structure of the hemoglobin was solved. Recombinant hemoglobin was expressed in Escherichia coli and was purified by ion-exchange chromatography. Recombinant hemoglobin was crystallized by the hanging-drop vapor-diffusion method using polyethylene glycol as a precipitant. The obtained orthorhombic crystal contained two subunits in the asymmetric unit. The refined structure was interpreted as the aquo-met form. Structural comparisons were performed among hemoglobins from deer mouse, house mouse and human. In contrast to human hemoglobin, deer mouse hemoglobin lacks the hydrogen bond between α1Trp14 in the A helix and α1Thr67 in the E helix owing to the Thr67Ala substitution. In addition, deer mouse hemoglobin has a unique hydrogen bond at the α1β1 interface between residues α1Cys34 and β1Ser128.

PubMed: 23545644
DOI: 10.1107/S1744309113005708

実験手法

X-RAY DIFFRACTION (1.779 Å)